ID F1MZ89_BOVIN Unreviewed; 1487 AA.
AC F1MZ89;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 2.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=ATP10A {ECO:0000313|Ensembl:ENSBTAP00000035070.5};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000035070.5, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000035070.5, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000035070.5,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000035070.5}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000035070.5};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00034036,
CC ECO:0000256|RuleBase:RU362033};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362033}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000256|ARBA:ARBA00008109,
CC ECO:0000256|RuleBase:RU362033}.
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DR RefSeq; XP_010815185.2; XM_010816883.2.
DR RefSeq; XP_010823085.2; XM_010824783.2.
DR STRING; 9913.ENSBTAP00000035070; -.
DR PaxDb; 9913-ENSBTAP00000035070; -.
DR Ensembl; ENSBTAT00000035192.5; ENSBTAP00000035070.5; ENSBTAG00000027081.5.
DR GeneID; 510723; -.
DR KEGG; bta:510723; -.
DR CTD; 57194; -.
DR VEuPathDB; HostDB:ENSBTAG00000027081; -.
DR eggNOG; KOG0206; Eukaryota.
DR GeneTree; ENSGT00940000157895; -.
DR HOGENOM; CLU_000846_3_4_1; -.
DR InParanoid; F1MZ89; -.
DR OMA; QALRCGR; -.
DR OrthoDB; 275833at2759; -.
DR TreeFam; TF354252; -.
DR Reactome; R-BTA-936837; Ion transport by P-type ATPases.
DR Proteomes; UP000009136; Chromosome 21.
DR Bgee; ENSBTAG00000027081; Expressed in trachea and 96 other cell types or tissues.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
DR CDD; cd02073; P-type_ATPase_APLT_Dnf-like; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 2.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006539; P-type_ATPase_IV.
DR InterPro; IPR032631; P-type_ATPase_N.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR032630; P_typ_ATPase_c.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01652; ATPase-Plipid; 2.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR24092:SF81; PHOSPHOLIPID-TRANSPORTING ATPASE VA; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362033};
KW Magnesium {ECO:0000256|RuleBase:RU362033};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362033};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362033};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362033};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362033};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362033}.
FT TRANSMEM 85..102
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 108..127
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 309..330
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 356..378
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1082..1102
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1114..1134
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1164..1187
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1193..1214
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1221..1241
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1266..1285
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 57..108
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1050..1295
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1308..1335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1352..1417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1459..1487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1487 AA; 165025 MW; 350D64714F7C14BC CRC64;
MEREPAAAAE EPGPPGRRRR REGRMRTVCS NLQPPPGAEE PAGKGAPRRR LRGGAQHLAD
NRLKTTKYTL LSFLPKNLFE QFHRLANVYF VFIALLNFVP AVNAFQPGLA LAPVLFILAV
TAFKDLWEDY SRHRSDHEIN HLGCLVFSRE EEQYVNRFWK EIRVGDFVRL RCNETIPADI
LLLSSSDPDG LCHIETANLD GETNLKRRQV VRGFSELVSE FNPLTFTSII ECEKPNNDLT
RFRGCIIHDN GKKAGLYKEN LLLRGCTLRN TEAVVGIVIY AGHETKALLN NSGPRYKRSR
LERQMNCDVL WCVLLLICMS LFSAIGHGLW VQRYQEKKSL FDVPESDGTS LSPVPAAVYS
FLTMIIVLQV LIPISLYVSI EIVKVCQVYF INQDIELYDE ETDSQLQCRA LNITEDLGQI
QYIFSDKTGT LTENKMVFRR CTVSGIEYSH DANAQRLARY QEADSEEEEV VPRGGSLPLR
GGTGGHPSAR AAHQSQSSRA HRRTGSRAEA RRVSMLTELT AFSSPMEKDV TPDPKLLEKV
HKCGRCLASA RHQEHPLDHL SPELSDIFDF FIALTICNTV VVTSPDQPRQ KVRVRFELKS
PVKTIEDFLR RFTPSRLTLG GSSVGSASMA AKSAPKASLL STMANDGALL RLEERLGPGA
PCLASNGYSS AADSWAAEQS ATGPEPGAEL RYEAESPDEA ALVHAARAYS CALVGRLHDQ
VSVELPHLGR LTFELLHTLG FDSIRKRMSV VIRHPLTDEI NVYTKGADSV VMDLLLPCST
DDARGRHQMK IRSKTQNYLN LYAVEGLRTL CIAKRVLSKE EYACWLQSHL EAESAVDNRE
ELLFQSAIRL ETNLHLLGAT GIEDRLQDGV PETIAKLRQA GLQIWVLTGD KQETAVNIAH
ACKLLDHDEE VITLNAESQE ACEALLDQCL RYVQSRSPQR TAGSLSVGFA PLCPPSEATA
SGPSLVIDGR SLAYALQKNL EDKFLFLAKQ CRSVLCCRST PLQKSMVVKL VRSKLKAMTL
AIGDGANDVS MIQVADVGVG ISGQEGMQAV MASDFAVPKF RYLERLLIVH GHWCYSRLAN
MVLYFFYKNT MFVGLLFWFQ FYCGFSASAM IDQWYLIFFN LLFSSLPQLV TGVLDKDVPA
DVLLAEPQLY RSGQNMEEYR PRTFWLNMAD AAFQSLVCFF IPYLAYYDSD TDIFTWGTPI
TAVALFTFLL HLGIETKTWT WLNWTACGFS VVLFFTVALI YNASCATCYP PSNPYWTMQT
LMGDPVFYSI CLLAPVAALL PRLFFKALQG TLFPTPLQLG RQLAKRSPGK FRAPRETSAQ
GHIPEEARTK LPGQRSVSVA RFVSRDCSSQ VSQGTWQPAC SPEAGGEPSA VDMGMPWREG
TLPDRLDSQP SRSSSPGPVA VEGCPGGSRM KPMSASRPAP LPSVFSVPGL SSLNWMSSLS
LVSGLGSVLQ FSRSGLPMDK RDSDFLPGSA PPDQDLCDLS GQTTDCF
//
